ID A0A317WPS2_9EURO Unreviewed; 4048 AA.
AC A0A317WPS2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BO70DRAFT_311035 {ECO:0000313|EMBL:PWY87651.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY87651.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY87651.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY87651.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY87651.1}.
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DR EMBL; MSFL01000006; PWY87651.1; -; Genomic_DNA.
DR STRING; 1448321.A0A317WPS2; -.
DR VEuPathDB; FungiDB:BO70DRAFT_311035; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3712..4048
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2065..2117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2355..2544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2583..2620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2838..2947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3010..3038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3092..3113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3313..3416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2458..2489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2499..2528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2838..2914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3010..3024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3313..3345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3351..3382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3390..3416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4015
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4048 AA; 451870 MW; 76CEF3E7CEEE9CC5 CRC64;
MGRIKKAASQ KHEATISPYL SEFVTRATTV PVPELPSHLN TFSRIWPFPR GDLYHWINVL
NRFDEILASV IEKYALNDGP QTKPFGRDFL VESCIQSEST ATPQDVDTKL ATLGYGAEGD
RELLEVIIDF SRLLLEKCGN RSLYSSSERL GELLNTTSLS LLQSTLRLSL CLAQRYHSRQ
RGGSHLQQSL LAAHYNIDLE KLQKIAAPFP RPFVLGRAAA SSPTATTKPK EKGPQTKHNA
NDMSSLVREK DGWDEWGNVR LLYYPSGVPE PVKNAPEVGA SGPSAQPTTP TPLRRSHTQP
TPRLSRMSTA EDSPTSVAGT PGKPDEGLQG GKTLDIPHSQ ISSSKPEDLL ALHADIPDDS
KYELLHRIRT AYGLATSSST REQILAIKIL ALTNLAYVYP EALFQQKVLQ YDMEQPKRLQ
LAYQLGELVH LGASGDLQVS RTLQTLAIHA LDALAKHKAR AIDVCAALSV NVNHGVLMFL
TRKTVNELGS EDGDGDDGSQ DEWRDALLAL LRTLPGSSTR TPETLVSAGL IPMFVDVLNL
RTEKARRVYS RIMEFLDTFV HAVRDALGTL TNAKGFDAIS DLIDFETKSS FESVSKGAGI
PAQHKTPSID YQIPYFQQQT LRWMFRFVNH IMQHNGGGFD RVLRNLIDSP QLLTSLRLVL
ENARIFGSHV WSNAVNILSS FIHNEPTSYA VIAEAGLSKS FLEAVTSSEL KTPEKPVVET
EDAQPEGESS KPADTGAAEK SADDGQKPQE YPVVRPKDVR LAPGIMSAAE ALSCIPAAFG
AICLNASGLD LFKSSDALES FFEIFENPEH VKCLKDDPNL VRTLGTTFDE LVRHHPALKS
HVMTAVIVMV ARVGLLCRTK AWSSGMGAKL WTEDTQGKPT ISGSTSHLLK AIGVDHDDQL
DNASTFGVPQ LTSSLLPNGG KLQMGDLDQI LPSSSDAIEP KDVDAAGLTA TDYLYPVVRF
LGAFFENQSN CQYFIESGAV EFVLDFATLQ SLPFDFHNTD ANQELAVLVH MLAETKPHLV
VPSLVHRTEL AIDKVSAFWK EPEYLGFFTP LIKPTSGNAS EEKGKEGLIT SKERGTYFAK
HMGAALILTD FLREIYSMPL YQTRPSQQTS AFAQVNLADR YRSLVKKLGG LHAACVWEEI
LLEKNIPDTW DQATKVQQSG TTPERTSLAP TNLNSEGSAT VAGAASAETP RESTVASDAP
QPGVAQEPKE TKVPEDGVAF KNVQALRYLL SSLPSSITGF FHNLGLGLIG KRRIDLYQKQ
NATMVAEAIA QAVIEQLQFQ PPNSSDSAKL RFAYLIVILS SFSHLLFEAT ADRPHSHYLT
LVLFAFKRQG GLKVMRDICE LFVQDVKALT PPESVSDSEK DVSARLTSAY GGIKIILSFF
SELASGKNIV DSSQTQAMTS SDRERDRPDY FQPGQFLVDL RMEILPMARD MWNSDFAAQS
SSSVVKCLVD ILRSSLDGEY ETGAARSSES APMWSDVPRR TFGINKDRLG TLLDRGFDAE
LAKEALYRCN NVFIAAEEYC RAQSWLRAPE RAEAPANDME QVRPTASGAE ASDEALGDAP
QFDSGFLERS ALAMLLAQAS GRSGEDGSRQ EQGQGRSEDS EVRHGTEFLA RALTHILNDE
HGPGDEHDDS SSLAPRNPSA AGVSSSEPSG QTANQSTEQR SEQPARRREL TTVEDLDKER
ETVRSNLIER CLDILNEHHD VSFELADLIA SATRRHRDPE SFRREVGEIL VQSLVSLQME
NFQAAGKKVA AYAHLLALVV QDRDMYTATL GELKECFTTF LGFIQVSNEK TADESFPWIG
HVLLVLEKLL SDDAQPPQIR WSLPDNANPE DEGPAHLEES LVSQDQKMQL YEALVEILPR
IGKDDTLALS ICRILVVLTR SRSIAVRLGE KRSLQRLFVM VKQLSSSTNE KLQGAFMLIL
RHIIEDEDTI RQIMRSEIVA NFESKSTRQV DTTGYVRQTY HLVLRSPELF VEISNEKLKL
QRYDSRQRPQ ILTLKSNKKN TPPDAPTTKE EAGDSSKTEE NQPSGASPSE DKGKGKATDL
KPPVVENPDG VIHYLLSELL SYKDVDDKES PAESTEAPAL EQSETQTDVE MSIDEPSPSV
ASTDAQGARN SKKSDKPTFK ADDHPIYIYR CFLLQCLTEL LSSYNRTKVE FINFSRKADP
LATTPSKPRS GILNYLLNVL VPIGTMEHDE SVAFKKRSNT SAWTMRVLVA LCTKTGEFGG
PGRRRNEQPL NEDDEPELAF VRRFVLEHAL RSYKEANSSN ESLDAKYSRL MSLADLFDKM
LSGYAFVSGD TAFPTSTRPL AKTMFEKHFI SALTASVAEI DLNFPASKRV IKYILRPLNK
LTQTAVLLSE SSDISTLGEA EDDDISSATS VSDMDDEREE TPDLFRHSTL GMLEPNHEEE
TSSEESEGDD DEMYDDEYDE EMDYEEEMAE DDGEVVSDEE DDDMGPIEGL PGDNGMDIEV
VLDDEDDDED DEDDDDEDDE SDMEDDEILA GEITGDHDND SLEEGDDDEW ESEDMSEDDE
EAEIMNQFED ELADSLRQAE QREDGQRFDD LFRVLNEAAG GVEDLQGDSL GDMHDDIVDD
DLAEEEEDEE LDELEEELED ADDDQGSYQG FDDEEDMAEP WGWEGDEHPP RGHHHHRFRG
TQPAWAAVTG IMPSRHGIVP IHPYRLHRTQ IPARGNDDGT NPLLVRADRG PEAAGQPRVP
GNEAFTDWVH GMEPMPNGRL LPMDSPVSFM NAIMQAIGGQ GGPGFGVITR PDGIHVHVNR
RAIVPNRIQD IFGLGRQQGP PSRTRDDPSQ AVSFALATTR SRWQEEAKIL FSTTFVEKSQ
RVVNSLLKIL VPPAMEEEKL REKQMEEERK RREEERAERE RQERIAKEEE EKERKRKEEE
ENARRQEEVE RQEAERQASG IETEPMDDVQ RTDTADEAAA PAPETETGPS EPTPRVHTTI
RGRQLDITGM EIDPEYLEAL PEELREEVIM QQLAEQRSQA AAAGEEPSEI NPEFLEALPA
EIREELLQQE AADRRRRERD TARRQTTTTA GAPPTIAEDM DAASFLATLN PSLRQAVLAD
QPDEILETLG PEFVTEARAL PGRRLTQFGD IPQVEHRHRH EPADDQEPKK QQRRQIVQML
DKAGVATLLR LMFMPLQGNA RHQLNDILHN VCENRQNRME VISLLLSVLQ DGSADVSAIE
RSFAQLSLRA KPSSVQKTPV KRNLSFQGSS NVSNEVTPIM VVQQCLGTLS FLSQYNPHIP
YFFLSEHDSS STLKLKAFRK GKGKENRANK FALNSLLTLL DRKLIMENPN CMEQLSSLLS
SITQPLTYLL RREKEKQEEE EKEKDKEKEK DKGKQSERTQ DEEATGEQQQ PEPAEPASAA
TDTTMTDAPL PTVETTAQNA GAEAQPEDGA SAEAAKEGKA KRTEEEKHKR RTIEPPVVPD
HNLQLVVHIL AARECNGKTF RDTLSTINNL SAVPGARDVI GNELVSQAQT LSTVILTDLD
ELLSHIHQAR TGTDMQGLAL AKFSPASSDQ AKLLRVLTAL DYLFDPSRAD KSKGIEQPDS
AAKEDVLQTL YECSTFGPLW TRLSECMSVI RQKENMLNVA TILLPLIEAL MVVCKNTTLK
DTSLARNSRE LSVSTTSVDA GLNMESLFFK FTEEHRKILN ELVRQNPRLM SGTFSLLVKN
PKVLEFDNKR NYFTRRIHSR GAEPRHPHPP LQLSVRRDQV FLDSFKSLYF KSADELKYGK
LNVRFHGEEG VDAGGVTREW FQVLARGMFN PNYALFIPVA SDRTTFHPNR LSGVNSEHLM
FFKFIGRIIG KALYEGRVLD CHFSRAVYKC ILGRSVSIKD METLDLDYYK SLLWMLENDI
TDIITETFAV ETDDFGEKQV IDLIEDGRNI PVTEENKEEY IQRVVDYRLV GSVKEQLDNF
LKGFHEIIPS DLISIFNEQE LELLISGLPE IEVDDWKVNT EYHNYSASSP QIQWFWRAVR
SFDKEERAKL LQFVTGTSKV PLNGFKELEG MNGVSRFNIH RDYGNKDRLP SSHTCFNQLD
LPEYESYETL RQRLYTAVTA GSEYFGFA
//
